Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A6ZW78 (GPI3_YEAS7)

Last modified January 19, 2010. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
    EC=2.4.1.198
Alternative name(s):
    GlcNAc-PI synthesis protein
Gene names
Name: SPT14
ORF Names: SCY_5555
OrganismSaccharomyces cerevisiae (strain YJM789) (Baker's yeast) [Complete proteome]
Taxonomic identifier307796 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis By similarity.

Catalytic activity

UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol.

Enzyme regulation

Inhibited by Ras, probably via the interaction between RAS2 and ERI1 By similarity.

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subunit structure

Component of the phosphatidylinositol N-acetylglucosaminyltransferase complex composed of at least GPI1, GPI2, GPI3, GPI15, GPI19 and ERI1 By similarity.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 1 family.

Ontologies

Keywords
   Biological processGPI-anchor biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processGPI anchor biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionphosphatidylinositol N-acetylglucosaminyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
PRO_0000377639

Regions

Transmembrane407 – 42721 Potential

Sequences

Sequence LengthMass (Da)Tools
A6ZW78-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: AAEB6D80967A7C7F

FASTA45251,316
        10         20         30         40         50         60 
MGFNIAMLCD FFYPQLGGVE FHIYHLSQKL IDLGHSVVII THAYKDRVGV RHLTNGLKVY 

        70         80         90        100        110        120 
HVPFFVIFRE TTFPTVFSTF PIIRNILLRE QIQIVHSHGS ASTFAHEGIL HANTMGLRTV 

       130        140        150        160        170        180 
FTDHSLYGFN NLTSIWVNKL LTFTLTNIDR VICVSNTCKE NMIVRTELSP DIISVIPNAV 

       190        200        210        220        230        240 
VSEDFKPRDP TDSTKRKQSR DKIVIVVIGR LFPNKGSDLL TRIIPKVCSS HEDVEFIVAG 

       250        260        270        280        290        300 
DGPKFIDFQQ MIESHRLQKR VQLLGSVPHE KVRDVLCQGD IYLHASLTEA FGTILVEAAS 

       310        320        330        340        350        360 
CNLLIVTTQV GGIPEVLPNE MTVYAEQTSV SDLVQATNKA INIIRSKALD TSSFHDSVSK 

       370        380        390        400        410        420 
MYDWMDVAKR TVEIYTNISS TSSADDKDWM KMVANLYKRD GIWAKHLYLL CGIVEYMLFF 

       430        440        450 
LLEWLYPRDE IDLAPKWPKK SVSNETKEAR ET 

« Hide

References

[1]"Genome sequencing and comparative analysis of Saccharomyces cerevisiae strain YJM789."
Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X., Jia P., Luedi P., Oefner P.J., David L. expand/collapse author list , Dietrich F.S., Li Y., Davis R.W., Steinmetz L.M.
Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007) [PubMed: 17652520] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFW02000135 Genomic DNA. Translation: EDN60970.1.

3D structure databases

SMRA6ZW78. Positions 3-385.
ModBaseSearch...

Phylogenomic databases

OrthoDBEOG9RR816.

Family and domain databases

InterProIPR001296. Glyco_trans_1.
IPR013234. PIGA_GPI_anchor_biosynthesis.
[Graphical view]
PfamPF00534. Glycos_transf_1. 1 hit.
PF08288. PIGA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGPI3_YEAS7
AccessionPrimary (citable) accession number: A6ZW78
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: September 11, 2007
Last modified: January 19, 2010
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents